CN111471733A - Preparation method and application of shark skin polypeptide dry powder - Google Patents
Preparation method and application of shark skin polypeptide dry powder Download PDFInfo
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- CN111471733A CN111471733A CN202010345273.5A CN202010345273A CN111471733A CN 111471733 A CN111471733 A CN 111471733A CN 202010345273 A CN202010345273 A CN 202010345273A CN 111471733 A CN111471733 A CN 111471733A
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- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 37
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 37
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 36
- 241000251730 Chondrichthyes Species 0.000 title claims abstract description 25
- 239000000843 powder Substances 0.000 title claims abstract description 18
- 238000002360 preparation method Methods 0.000 title claims abstract description 14
- 102000004190 Enzymes Human genes 0.000 claims abstract description 10
- 108090000790 Enzymes Proteins 0.000 claims abstract description 10
- 239000002537 cosmetic Substances 0.000 claims abstract description 7
- 235000013376 functional food Nutrition 0.000 claims abstract description 7
- 230000003078 antioxidant effect Effects 0.000 claims abstract description 6
- 239000003963 antioxidant agent Substances 0.000 claims abstract description 4
- 238000005520 cutting process Methods 0.000 claims abstract description 4
- 238000001914 filtration Methods 0.000 claims abstract description 4
- 238000004108 freeze drying Methods 0.000 claims abstract description 4
- 238000009777 vacuum freeze-drying Methods 0.000 claims abstract description 3
- 108091005804 Peptidases Proteins 0.000 claims abstract 3
- 239000004365 Protease Substances 0.000 claims abstract 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 10
- 241001061264 Astragalus Species 0.000 claims description 7
- 238000005238 degreasing Methods 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 5
- 241000258957 Asteroidea Species 0.000 claims description 4
- 239000007853 buffer solution Substances 0.000 claims description 3
- 238000005119 centrifugation Methods 0.000 claims 2
- 230000009849 deactivation Effects 0.000 claims 2
- 239000008055 phosphate buffer solution Substances 0.000 claims 1
- 238000005406 washing Methods 0.000 claims 1
- 241000251468 Actinopterygii Species 0.000 abstract description 14
- 241000244203 Caenorhabditis elegans Species 0.000 abstract description 9
- 238000004140 cleaning Methods 0.000 abstract description 6
- 230000036542 oxidative stress Effects 0.000 abstract description 6
- 241000257468 Asterias amurensis Species 0.000 abstract description 5
- 230000000415 inactivating effect Effects 0.000 abstract description 2
- 235000000019 Astrocaryum vulgare Nutrition 0.000 abstract 1
- 241000454556 Astrocaryum vulgare Species 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 6
- 238000002835 absorbance Methods 0.000 description 5
- 230000004083 survival effect Effects 0.000 description 5
- 230000013632 homeostatic process Effects 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000006227 byproduct Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 230000007760 free radical scavenging Effects 0.000 description 2
- KQPYUDDGWXQXHS-UHFFFAOYSA-N juglone Chemical compound O=C1C=CC(=O)C2=C1C=CC=C2O KQPYUDDGWXQXHS-UHFFFAOYSA-N 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 150000003254 radicals Chemical class 0.000 description 2
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 208000024827 Alzheimer disease Diseases 0.000 description 1
- 235000008845 Astrocaryum Nutrition 0.000 description 1
- 241001299959 Astrocaryum Species 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 241001257016 Platyphylla Species 0.000 description 1
- 230000002292 Radical scavenging effect Effects 0.000 description 1
- 241001274981 Siganus canaliculatus Species 0.000 description 1
- 241000041303 Trigonostigma heteromorpha Species 0.000 description 1
- VYTBDSUNRJYVHL-UHFFFAOYSA-N beta-Hydrojuglone Natural products O=C1CCC(=O)C2=C1C=CC=C2O VYTBDSUNRJYVHL-UHFFFAOYSA-N 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000003891 ferrous sulphate Nutrition 0.000 description 1
- 239000011790 ferrous sulphate Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000007407 health benefit Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 1
- 238000005502 peroxidation Methods 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 229960004889 salicylic acid Drugs 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- 230000002000 scavenging effect Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 235000014102 seafood Nutrition 0.000 description 1
- 239000002910 solid waste Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000001360 synchronised effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A40/00—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production
- Y02A40/90—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production in food processing or handling, e.g. food conservation
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Abstract
The invention provides a preparation method of a dry powder of a shark skin polypeptide and application of the polypeptide in preparing functional foods and cosmetics. The preparation method comprises cleaning the skin of Astrocaryum vulgare, cutting into small pieces, defatting, filtering, repeatedly cleaning, freeze drying, performing enzymolysis with protease to obtain primary extract, inactivating enzyme, centrifuging, and vacuum freeze drying to obtain dry powder. The asterias amurensis fish skin polypeptide dry powder provided by the invention has good antioxidant activity, can obviously reduce the oxidative stress of caenorhabditis elegans, can be used as a functional factor and applied to antioxidant functional foods and cosmetics.
Description
Technical Field
The invention relates to preparation and application of animal-derived functional polypeptide dry powder, and particularly belongs to a preparation method of a astragal fish skin polypeptide and application of the prepared astragal fish skin polypeptide in preparation of antioxidant functional foods and cosmetics.
Background
Shark (Mustellus cantis) is a small edible shark, mainly produced in the western Atlantic region. The shark skin is very tough and solid waste generated in seafood processing. Since the skin of the shark harlequin contains a large amount of collagen, it is an excellent source of bioactive peptides.
Cellular redox homeostasis plays a crucial role in homeostasis. Disorders of redox homeostasis are the underlying mechanisms of many diseases, including cardiovascular disease, type 2 diabetes, cancer and alzheimer's syndrome. Excess ROS cause peroxidation of biological macromolecules (DNA, proteins, RNA, and lipids), leading to a collapse of the redox homeostasis. Antioxidants can provide health benefits to the body by scavenging excess free radicals or otherwise hindering the synthesis of free radicals. Finding and screening substances with antioxidant activity from byproducts of agricultural or fishery processing has attracted a great deal of attention. Therefore, the method of enzymolysis is utilized to prepare the active polypeptide from the fishery processing by-product-the shark skin, the functional mechanism of the active polypeptide is determined, and valuable functional food or cosmetics are developed.
Disclosure of Invention
The invention aims to provide a preparation method of a dry powder of a shark skin polypeptide and application of the polypeptide in preparing functional foods or cosmetics.
In order to achieve the purpose, the invention provides the following technical scheme:
the invention provides a dry powder of astragal skin polypeptide, which is prepared by the following steps of cleaning the skin of astragal fish for a plurality of times, cutting the skin of astragal fish into small pieces of 0.5 × 0.5.5 cm, adding 95% ethanol with 5 times of volume, degreasing for 12h, filtering to remove the ethanol, repeatedly cleaning for a plurality of times, freeze-drying, adding Sea-B-Zyme L200 enzyme at 50 ℃, wherein the feed-liquid ratio of the skin of astragal fish to a buffer solution is 1:16-1:20g/m L, the enzyme addition amount is 4000-.
The asterias amurensis fish skin polypeptide dry powder provided by the invention has good in-vitro antioxidant activity.
The invention provides the asterias amurensis fish skin polypeptide dry powder which improves the survival rate of caenorhabditis elegans under oxidative stress conditions.
Compared with the prior art, the invention separates and prepares the asterias amurensis fish skin polypeptide dry powder from the fishery processing byproduct, namely the asterias amurensis fish skin for the first time, and the polypeptide can obviously improve the survival rate of the caenorhabditis elegans under the oxidative stress condition. The preparation of the polypeptide and the discovery of the function of the polypeptide have great economic value for the deep development and the comprehensive utilization of the shark skin resource, and simultaneously provide technical support for the development of related functional foods or cosmetics.
Drawings
FIG. 1 shows OH radical scavenging ability of shark skin polypeptide
FIG. 2 is a graph showing the effect of shark skin polypeptide on survival rate under oxidative stress conditions of caenorhabditis elegans
Detailed Description
To further illustrate the technical means and effects of the present invention, the following further describes the technical solutions of the present invention by way of specific embodiments with reference to the drawings, but the present invention is not limited to the scope of the embodiments.
The examples do not show the specific techniques or conditions, according to the technical or conditions described in the literature in the field, or according to the product specifications. The reagents or instruments used are conventional products available from regular distributors, not indicated by the manufacturer.
Example 1: preparation of dry powder of shark skin polypeptide
The method comprises the following steps of manually separating fish skin from fish meat, cleaning the fish skin of the starfish for a plurality of times, cutting the fish skin into small pieces of 0.5 × 0.5.5 cm, adding 95% ethanol with 5 times of volume, degreasing for 12 hours, filtering to remove the ethanol, repeatedly cleaning for 6 times, freeze-drying, accurately weighing 20g of the starfish skin, adding a proper amount of phosphate buffer (pH 7) to enable the final volume of a reaction system to be 360m L, adding the enzyme of Sea-B-Zyme L200 with the amount of 4000U/g, the enzymolysis temperature being 50 ℃, the enzymolysis time being 6 hours, inactivating the enzyme at 100 ℃ for 5 minutes after the enzymolysis reaction is finished, centrifuging for 15 minutes at 8000r/min, and carrying out vacuum freeze-drying to obtain the starfish skin polypeptide dry powder.
Example 2: OH free radical scavenging ability of Astrocaryum platypomum skin polypeptide
The test is carried out by adding 6 mmol/L ferrous sulfate solution 2.0m L, different concentrations of Astrocarya platyphylla skin polypeptide solution 2.0m L, 6 mmol/L hydrogen peroxide solution 2.0m L into 10m L test tube, shaking, standing for 10min, adding 6 mmol/L salicylic acid solution 2.0m L, shaking, standing for 30min, measuring absorbance at 510nm, and repeating measuring for 3 times.
Clearance/% ([ 1- (a) ]S－AX)/A0]×100
In the formula: a. the0The absorbance is the background absorbance without adding sample liquid; a. theSIs the absorbance after adding the sample solution for reaction; a. theXThe absorbance of the salicylic acid-free solution was obtained.
Experiments show that the siganus oramin skin polypeptide has good OH free radical scavenging capacity (shown in figure 1).
Example 3: effect of shark skin polypeptide on survival rate of caenorhabditis elegans under oxidative stress condition
The caenorhabditis elegans synchronized to L2 stage is transferred to NGM culture medium containing 30 mu g/M L star shark skin polypeptide, a control group is arranged, after two days of culture, the caenorhabditis elegans is transferred to NGM plate of 240 mu M Juglone, counting is started until the caenorhabditis elegans are all dead, and experimental results show that the star shark skin polypeptide improves the survival rate of the caenorhabditis elegans under oxidative stress conditions (see figure 2).
The above embodiments are merely illustrative, and not restrictive, and various changes and modifications may be made by those skilled in the art without departing from the spirit and scope of the invention, and therefore all equivalent technical solutions are intended to be included within the scope of the invention.
Claims (7)
1. A preparation method of a dry powder of shark skin polypeptide is characterized by comprising the following steps:
s1, cutting the clean shark skin into small pieces, and degreasing;
s2, filtering the degreased shark skin, repeatedly washing for 3-6 times, and freeze-drying;
s3, carrying out enzymolysis on the shark skin by adopting protease to obtain a primary extract of the shark skin polypeptide;
s4, carrying out enzyme deactivation and centrifugation on the primary extract of the shark skin polypeptide, and carrying out vacuum freeze drying to obtain the dry powder of the shark skin polypeptide.
2. The method of claim 1, wherein the degreasing in step S1 is performed by using 95% ethanol with 5 times volume of degreasing time being 12 h.
3. The preparation method of claim 1, wherein the protease in step S3 is Sea-B-Zyme L200 enzyme, the enzymolysis condition of the enzyme is that the ratio of the starfish skin to the buffer solution is 1:16-20g/m L, the enzyme amount is 4000-4500U/g, the enzymolysis temperature is 50 ℃, the enzymolysis time is 6-7h, and the buffer solution is phosphate buffer solution with pH 7.
4. The method according to claim 1, wherein the enzyme deactivation centrifugation treatment in step S4 is carried out at 100 ℃ for 2-5min and 8000r/min for 15-30 min.
5. A dry astragal skin polypeptide powder, which is prepared by the preparation method of any one of claims 1 to 4.
6. The use of the dry powder of the shark skin polypeptide of claim 5 in the preparation of an antioxidant functional food.
7. The use of the dry powder of the shark skin polypeptide as claimed in claim 5 in cosmetics.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010345273.5A CN111471733B (en) | 2020-04-27 | 2020-04-27 | Preparation method and application of shark skin polypeptide dry powder |
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| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202010345273.5A CN111471733B (en) | 2020-04-27 | 2020-04-27 | Preparation method and application of shark skin polypeptide dry powder |
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| Publication Number | Publication Date |
|---|---|
| CN111471733A true CN111471733A (en) | 2020-07-31 |
| CN111471733B CN111471733B (en) | 2023-03-07 |
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Citations (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2003284586A (en) * | 2002-03-28 | 2003-10-07 | Jellice Co Ltd | Method for producing collagen peptide and method for producing product utilizing the same |
| CN101538602A (en) * | 2009-04-13 | 2009-09-23 | 湖北瑞邦生物科技有限公司 | Extraction method of fish skin collagen |
| CN103409489A (en) * | 2013-08-15 | 2013-11-27 | 集美大学 | Preparation method for fish collagen antioxidant peptide |
| CN103524597A (en) * | 2012-07-03 | 2014-01-22 | 浙江海洋学院 | Antioxidant peptide prepared from shark prolamin and preparation method and application thereof |
| CN103627768A (en) * | 2013-12-05 | 2014-03-12 | 福州大学 | Fish skin collagen bioactive small peptide and preparation method thereof |
| CN105907823A (en) * | 2016-05-05 | 2016-08-31 | 广东海洋大学 | Tilapia skin protein peptide and preparation method and application thereof |
| CN108715879A (en) * | 2018-05-31 | 2018-10-30 | 厦门肽王基因科技有限公司 | A kind of ash gummy shark mixed type polypeptide and its preparation method and application |
| CN111676262A (en) * | 2020-07-10 | 2020-09-18 | 厦门肽王基因科技有限公司 | Shark composite short peptide with anti-inflammatory activity, preparation method and application |
| US20220145349A1 (en) * | 2018-06-26 | 2022-05-12 | Fu Zhou University | Preparation method of anti-oxidation polypeptide |
-
2020
- 2020-04-27 CN CN202010345273.5A patent/CN111471733B/en active Active
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| JP2003284586A (en) * | 2002-03-28 | 2003-10-07 | Jellice Co Ltd | Method for producing collagen peptide and method for producing product utilizing the same |
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